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1. Compound ID: 48
|
b-D-Galp-(1-4)-b-D-GlcNAc-(1--/(CH2)8CO2CH3 or para-nitrothiophenyl/ |
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Structure type: oligomer
Aglycon: (CH2)8CO2CH3 or para-nitrothiophenyl
Contained glycoepitopes: IEDB_130646,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_151531,IEDB_190606,SB_165,SB_166,SB_187,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 17
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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2. Compound ID: 49
Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 17
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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3. Compound ID: 69
Structure type: oligomer
Aglycon: (CH2)8CO2CH3
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,SB_165,SB_166,SB_187,SB_195,SB_30,SB_40,SB_7,SB_87,SB_88
The structure is contained in the following publication(s):
- Article ID: 17
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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4. Compound ID: 1107
|
-2)-a-L-Rhap-(1-2)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-GlcNAc-(1- |
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Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_125613,IEDB_125614,IEDB_127514,IEDB_133752,IEDB_133753,IEDB_133754,IEDB_135813,IEDB_135849,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_141815,IEDB_141816,IEDB_143253,IEDB_151531,IEDB_153213,IEDB_225177,IEDB_885823
The structure is contained in the following publication(s):
- Article ID: 333
Morona R, Macpherson DF, Van den Bosch L, Carlin NIA, Manning PA "Lipopolysaccharide with an altered O-antigen produced in Escherichia coli K-12 harbouring mutated, cloned Shigella flexneri rfb genes" -
Molecular Microbiology 18 (1995) 209-223
Cloning of the rfb genes of Shigella flexneri 2a into Escherichia coli K-12 strain DH1 results in the synthesis of lipopolysaccharides (LPS) with an O-antigen chain having type antigen IV and group antigens 3,4. During genetic studies of these rfb genes in E. coli K-12, we observed that strains harbouring plasmids with certain mutations (inversion and transposon insertions) which should have blocked O-antigen synthesis nevertheless still produced LPS with O-antigen chains. These LPS migrated differently on silver-stained SDSpolyacrylamide gels, compared with the LPS produced by wild-type rfb genes, and the group 3,4 antigens were barely detectable, suggesting that the O-antigen was altered. Investigation of the genetic determinants for production of the altered O-antigen/LPS indicated that: (i) these LPS are produced as a result of mutations which are either polar on rfbF or inactivate rfbF; (ii) the rfbX gene product (or a similar protein in the E. coli K-12 rfb region) is needed for production of the altered O-antigen in the form of LPS; (iii) the rfbG gene product is required for the production of both the parental and altered LPS; (iv) the dTDP-rhamnose biosynthesis genes are required. Additionally, an E. coli K-12 gene product(s) encoded outside the rfb region also contributes to production of the O-antigen of the altered LPS. An antiserum raised to the altered LPS from strain DH1(pPM2217 (rfbX::Tn1725)) was found to cross-react with nearly all S. flexneri serotypes, and with the altered LPS produced by other DH1 strains harbouring plasmids with different rfb mutations, as described above. The reactivity of the altered LPS with a panel of monoclonal antibodies specific for various S. flexneri O-antigen type and group antigens demonstrated that their O-antigen components were closely related to that of S. flexneri serotype 4. The RfbF and RfbG proteins were shown to have similarity to rhamnose transferases, and we identified a motif common to the N-termini of 6-deoxy-hexose nucleotide sugar transferases. We propose that the E. coli K-12 strains harbouring the mutated S. flexneri rfb genes produce LPS with a hybrid O-antigen as a consequence of inactivation of RfbF and complementation by an E. coli K-12 gene product. Analysis of the genetic and immunochemical data suggested a possible structure for the O-antigen component of the altered LPS.
LPS, gene, O-antigen, Escherichia, Escherichia coli, rfb, Shigella flexneri, Shigella, cloned
NCBI PubMed ID: 8709841Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: RMORONA@MICROB.ADELAIDE.EDU.AU
Institutions: Microbial Pathogenesis Unit, Department of Microbiology and Immunology, University of Adelaide, Adelaide, South Australia, Australia, 5005, SBL Vaccin AB, S-105 21 Stockholm, Sweden
Methods: DNA sequencing, SDS-PAGE, ELISA, immunoblotting, agglutination, passive hemagglutination
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5. Compound ID: 1108
|
-2)-a-L-Rhap-(1-3)-a-L-Rhap-(1-2)-a-D-Galp-(1-3)-b-D-GlcNAc-(1- |
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Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_125611,IEDB_130669,IEDB_135813,IEDB_136105,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_143253,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_225177,IEDB_885823,SB_7
The structure is contained in the following publication(s):
- Article ID: 333
Morona R, Macpherson DF, Van den Bosch L, Carlin NIA, Manning PA "Lipopolysaccharide with an altered O-antigen produced in Escherichia coli K-12 harbouring mutated, cloned Shigella flexneri rfb genes" -
Molecular Microbiology 18 (1995) 209-223
Cloning of the rfb genes of Shigella flexneri 2a into Escherichia coli K-12 strain DH1 results in the synthesis of lipopolysaccharides (LPS) with an O-antigen chain having type antigen IV and group antigens 3,4. During genetic studies of these rfb genes in E. coli K-12, we observed that strains harbouring plasmids with certain mutations (inversion and transposon insertions) which should have blocked O-antigen synthesis nevertheless still produced LPS with O-antigen chains. These LPS migrated differently on silver-stained SDSpolyacrylamide gels, compared with the LPS produced by wild-type rfb genes, and the group 3,4 antigens were barely detectable, suggesting that the O-antigen was altered. Investigation of the genetic determinants for production of the altered O-antigen/LPS indicated that: (i) these LPS are produced as a result of mutations which are either polar on rfbF or inactivate rfbF; (ii) the rfbX gene product (or a similar protein in the E. coli K-12 rfb region) is needed for production of the altered O-antigen in the form of LPS; (iii) the rfbG gene product is required for the production of both the parental and altered LPS; (iv) the dTDP-rhamnose biosynthesis genes are required. Additionally, an E. coli K-12 gene product(s) encoded outside the rfb region also contributes to production of the O-antigen of the altered LPS. An antiserum raised to the altered LPS from strain DH1(pPM2217 (rfbX::Tn1725)) was found to cross-react with nearly all S. flexneri serotypes, and with the altered LPS produced by other DH1 strains harbouring plasmids with different rfb mutations, as described above. The reactivity of the altered LPS with a panel of monoclonal antibodies specific for various S. flexneri O-antigen type and group antigens demonstrated that their O-antigen components were closely related to that of S. flexneri serotype 4. The RfbF and RfbG proteins were shown to have similarity to rhamnose transferases, and we identified a motif common to the N-termini of 6-deoxy-hexose nucleotide sugar transferases. We propose that the E. coli K-12 strains harbouring the mutated S. flexneri rfb genes produce LPS with a hybrid O-antigen as a consequence of inactivation of RfbF and complementation by an E. coli K-12 gene product. Analysis of the genetic and immunochemical data suggested a possible structure for the O-antigen component of the altered LPS.
LPS, gene, O-antigen, Escherichia, Escherichia coli, rfb, Shigella flexneri, Shigella, cloned
NCBI PubMed ID: 8709841Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: RMORONA@MICROB.ADELAIDE.EDU.AU
Institutions: Microbial Pathogenesis Unit, Department of Microbiology and Immunology, University of Adelaide, Adelaide, South Australia, Australia, 5005, SBL Vaccin AB, S-105 21 Stockholm, Sweden
Methods: DNA sequencing, SDS-PAGE, ELISA, immunoblotting, agglutination, passive hemagglutination
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6. Compound ID: 1129
|
a-Galp-(1-6)-+
|
/Variants 0/-a-Glcp-(1-2)-a-Glcp-(1-3)-a-Glcp
/Variants 0/ is:
b-GlcpNAc-(1-6)-
OR (exclusively)
a-Hepp-(1-6)- |
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Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_135813,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 339
Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" -
Journal of Medical Microbiology 48(5) (1999) 433-441
To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.
Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae
NCBI PubMed ID: 10229540Journal NLM ID: 0224131Publisher: Reading, England: Society for General Microbiology
Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
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7. Compound ID: 1972
Structure type: oligomer
; 513 [M+H]+ permethylated
Aglycon: D-Gal-ol-1-d
Contained glycoepitopes: IEDB_114704,IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531
The structure is contained in the following publication(s):
- Article ID: 616
Aspinall GO, Mainkar AS, Moran AP "A structural comparison of lipopolysaccharides from two strains of Helicobacter pylori, of which one strain (442) does and the other strain (471) does not stimulate pepsinogen secretion" -
Glycobiology 9(11) (1999) 1235-1245
Lipopolysaccharides (LPSs) from strains of Helicobacter pylori (442 and 471), which differed in stimulation of pepsinogen secretion, were isolated as water-soluble material of high-Mr, and as water-insoluble gels of low-Mr. Chemical and spectroscopic analyses of soluble LPS and oligosaccharides liberated from the gels led to proposed structures with Lewis (Le) antigen termini connected to N-acetyllactosaminoglycans of alternating 3-linked b-D-Gal and 4-linked b-D-GlcNAc residues with various laterally attached glycosyl substituents. The LPS of H.pylori 442 was similar to previously examined strains (NCTC11637 and P466) in having partially glycosylated chains with a-L-Fuc units attached to O-3 of the majority of GlcNAc residues in Lex units, and in chain termination with Lex or Ley determinants. In contrast, terminal Ley units occurred in LPS of H.pylori 471 and glycosaminoglycan chains carried a smaller proportion of a-L-Fuc units, but at O-6 of a majority of nonfucosylated GlcNAc residues, there was a novel type of branching with a-D-Gal substituents. Evidence for the branched regions was obtained from 1H NMR spectra and from characterization of oligosaccharides formed by the action of endo-β-galactosidase. Examination of oligosaccharides liberated from water-insoluble LPS gels of H.pylori 442 and 471 provided evidence for similar core OS structures to those from other H.pylori strains but interesting differences were observed.
Lipopolysaccharide, lipopolysaccharides, strain, structural, Helicobacter pylori, comparison, Helicobacter, pepsinogen, secretion
NCBI PubMed ID: 10536039Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Microbiology, National University of Ireland, Galway, Ireland, Department of Chemistry, York University, North York, ON M3J 1P3, Canada
Methods: NMR-2D, FAB-MS, Smith degradation, enzymatic degradation, defucosylation
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8. Compound ID: 2054
|
b-D-GlcNAc-(1-3)-+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
| | |
D-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130670,IEDB_135813,IEDB_137340,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 659
Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP "The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature" -
Advances in Experimental Medicine and Biology 529 (2003) 229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID: 12756762Journal NLM ID: 0121103Publisher: Kluwer Academic/Plenum Publishers
Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany
Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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9. Compound ID: 2168
|
b-D-GlcNAc-(1-3)-+ b-D-Glcp-(1-4)-+ a-Kop-(2-4)-+
| | |
D-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_130650,IEDB_130670,IEDB_135607,IEDB_135609,IEDB_135813,IEDB_137340,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 659
Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP "The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature" -
Advances in Experimental Medicine and Biology 529 (2003) 229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID: 12756762Journal NLM ID: 0121103Publisher: Kluwer Academic/Plenum Publishers
Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany
Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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10. Compound ID: 2169
|
b-D-GlcNAc-(1-3)-+ b-D-Glcp-(1-4)-+ a-Kop-(2-4)-+
| | |
b-D-Galp-(1-7)-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_130650,IEDB_130670,IEDB_135607,IEDB_135609,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 659
Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP "The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature" -
Advances in Experimental Medicine and Biology 529 (2003) 229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID: 12756762Journal NLM ID: 0121103Publisher: Kluwer Academic/Plenum Publishers
Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany
Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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11. Compound ID: 2170
|
b-D-GlcNAc-(1-3)-+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
| | |
b-D-Galp-(1-7)-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130670,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 659
Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP "The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature" -
Advances in Experimental Medicine and Biology 529 (2003) 229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID: 12756762Journal NLM ID: 0121103Publisher: Kluwer Academic/Plenum Publishers
Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany
Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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12. Compound ID: 2171
|
b-D-GlcNAc-(1-3)-+ b-D-Glcp-(1-4)-+ a-Kop-(2-4)-+
| | |
b-D-Galp-(1-7)-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
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Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130670,IEDB_135607,IEDB_135609,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 659
Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP "The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature" -
Advances in Experimental Medicine and Biology 529 (2003) 229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID: 12756762Journal NLM ID: 0121103Publisher: Kluwer Academic/Plenum Publishers
Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany
Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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13. Compound ID: 2172
|
b-D-GlcNAc-(1-3)-+ b-D-Glcp-(1-4)-+ a-Kop-(2-4)-+
| | |
D-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130670,IEDB_135607,IEDB_135609,IEDB_135813,IEDB_137340,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 659
Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP "The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature" -
Advances in Experimental Medicine and Biology 529 (2003) 229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID: 12756762Journal NLM ID: 0121103Publisher: Kluwer Academic/Plenum Publishers
Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany
Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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14. Compound ID: 2173
|
b-D-GlcNAc-(1-3)-+ b-D-Glcp-(1-4)-+
| |
D-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130670,IEDB_135813,IEDB_137340,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 659
Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP "The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature" -
Advances in Experimental Medicine and Biology 529 (2003) 229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID: 12756762Journal NLM ID: 0121103Publisher: Kluwer Academic/Plenum Publishers
Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany
Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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15. Compound ID: 2174
|
b-D-GlcNAc-(1-3)-+ b-D-Glcp-(1-4)-+
| |
b-D-Gal-(1-7)-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130670,IEDB_135813,IEDB_136044,IEDB_136095,IEDB_137340,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 659
Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP "The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature" -
Advances in Experimental Medicine and Biology 529 (2003) 229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID: 12756762Journal NLM ID: 0121103Publisher: Kluwer Academic/Plenum Publishers
Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany
Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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Next 15 structure(s)
Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (permanent record IDs):
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